GenomeNet

Database: UniProt
Entry: BGALC_ASPFN
LinkDB: BGALC_ASPFN
Original site: BGALC_ASPFN 
ID   BGALC_ASPFN             Reviewed;         984 AA.
AC   B8N2I5;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   16-JAN-2019, entry version 54.
DE   RecName: Full=Probable beta-galactosidase C;
DE            EC=3.2.1.23;
DE   AltName: Full=Lactase C;
DE   Flags: Precursor;
GN   Name=lacC; ORFNames=AFLA_037600;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM
OS   12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167;
RX   PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
CC   -!- FUNCTION: Cleaves beta-linked terminal galactosyl residues from
CC       gangliosides, glycoproteins, and glycosaminoglycans.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose
CC         residues in beta-D-galactosides.; EC=3.2.1.23;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000305}.
DR   EMBL; EQ963473; EED56486.1; -; Genomic_DNA.
DR   RefSeq; XP_002375268.1; XM_002375227.1.
DR   ProteinModelPortal; B8N2I5; -.
DR   SMR; B8N2I5; -.
DR   PRIDE; B8N2I5; -.
DR   EnsemblFungi; EED56486; EED56486; AFLA_037600.
DR   GeneID; 7919723; -.
DR   KEGG; afv:AFLA_037600; -.
DR   EuPathDB; FungiDB:AFLA_037600; -.
DR   HOGENOM; HOG000181922; -.
DR   OMA; EFEGGWF; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.102.20.10; -; 1.
DR   Gene3D; 2.60.120.260; -; 2.
DR   Gene3D; 2.60.390.10; -; 1.
DR   InterPro; IPR018954; Betagal_dom2.
DR   InterPro; IPR037110; Betagal_dom2_sf.
DR   InterPro; IPR025972; BetaGal_dom3.
DR   InterPro; IPR036833; BetaGal_dom3_sf.
DR   InterPro; IPR025300; BetaGal_jelly_roll_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR23421; PTHR23421; 1.
DR   Pfam; PF10435; BetaGal_dom2; 1.
DR   Pfam; PF13363; BetaGal_dom3; 1.
DR   Pfam; PF13364; BetaGal_dom4_5; 2.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SMART; SM01029; BetaGal_dom2; 1.
DR   SUPFAM; SSF117100; SSF117100; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Complete proteome; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   CHAIN        24    984       Probable beta-galactosidase C.
FT                                /FTId=PRO_0000395236.
FT   ACT_SITE    188    188       Proton donor. {ECO:0000255}.
FT   ACT_SITE    287    287       Nucleophile. {ECO:0000255}.
FT   BINDING      82     82       Substrate. {ECO:0000250}.
FT   BINDING     127    127       Substrate. {ECO:0000250}.
FT   BINDING     128    128       Substrate; via amide nitrogen.
FT                                {ECO:0000250}.
FT   BINDING     129    129       Substrate. {ECO:0000250}.
FT   BINDING     187    187       Substrate. {ECO:0000250}.
FT   BINDING     251    251       Substrate. {ECO:0000250}.
FT   BINDING     353    353       Substrate. {ECO:0000250}.
FT   CARBOHYD    197    197       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    276    276       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    391    391       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    421    421       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    434    434       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    517    517       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    602    602       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    677    677       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    715    715       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    720    720       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    759    759       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    805    805       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    257    304       {ECO:0000250}.
SQ   SEQUENCE   984 AA;  108670 MW;  3E91614086ACDEB2 CRC64;
     MRLLSFIYLV WLALLTGTPQ VSATDNGKTS DVAWDKYSLS VKGERLFVFS GEFHYQRLPV
     PELWLDVFQK LRANGFNTIS VYFFWSYHSA SEDVFDFTTG AHDIQRLFDY AKQAGLYVIA
     RAGPYCNAET SAGGFALWAA NGQMGSERTS DEAYYKKWKP WILEVGKIIA ANQITNGGPV
     ILNQHENELQ ETTYDSNDTK VIYMEQVAKA FEEAGVVVPS SHNEKGMRTV SWSTDYKNVG
     GAVNVYGLDS YPGSLSCANP NSGFNLLRTY YQWFQNYSYT QPEYLAEFEG GWFQPWGGSF
     YDSCASELSP EFADVYYKNN IGSRVTLHNI YMTFGGTNWG HSAAPVVYTS YDYGSPLRET
     REIRDKLKQT KLLGLFTRVS KDLLKTYMEG NGTSYTSDDS IYTWALRNPD SDAGFYVVAH
     NTSSSREVTT FSLNITTSAG ALTIPDIELD GRQSKIIVTD YSIGSESSLL YSSAEVLTYA
     TLDVDVLVFY LNAGQKGAFV FKDAPADLKY QTYGNSNLSA LETSQGTQYS YTQGEGVTAV
     KFSNGVLVYL LDKETAWNFF APPTVSSPTV APNEHILVFG PYLVRGASIK HDTVEIVGDN
     SNSTSIEIYT GDEHVKKVSW NGNLIDTRAT AYGSLIGTVP GAEDIEISLP SLSSWKAQDT
     LPEISPDYDD SRWTICNKTT SVNSVAPLSL PVLYSGDYGY HTGTKIYRGR FDGQNATGAN
     VTVQNGVAAG WAAWLNGAYV GGFSGDPDKV ASWEVLKFNH SSLRSRDNVL TIITDYTGHD
     QNSQKPIGTQ NPRGIMGATL IGGGNFTLWR IQGNAGGEKN IDPVRGPMNE GGLYGERMGW
     HLPGYQVPES ALDSSPLEGV SGAEGRFYTT SFQLDLEEDL DVPIGLQLSA PAGTEAVVQI
     FMNGYQFGHY LPHIGPQSLF PFPPGVIYNR GQNSLAISMW ALTDAGARLE QVELKAYAKY
     RSGFDFNRDW TYLQPGWKDR TEYA
//
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